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Entry: A0A221M7Z0_9BACI
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ID   A0A221M7Z0_9BACI        Unreviewed;       214 AA.
AC   A0A221M7Z0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   08-MAY-2019, entry version 10.
DE   RecName: Full=Thymidylate kinase {ECO:0000256|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000256|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000256|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165};
GN   ORFNames=CFK40_01460 {ECO:0000313|EMBL:ASN03763.1};
OS   Virgibacillus necropolis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=163877 {ECO:0000313|EMBL:ASN03763.1, ECO:0000313|Proteomes:UP000204391};
RN   [1] {ECO:0000313|EMBL:ASN03763.1, ECO:0000313|Proteomes:UP000204391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 19488 {ECO:0000313|EMBL:ASN03763.1,
RC   ECO:0000313|Proteomes:UP000204391};
RX   PubMed=12710619; DOI=10.1099/ijs.0.02371-0;
RA   Heyrman J., Logan N.A., Busse H.J., Balcaen A., Lebbe L.,
RA   Rodriguez-Diaz M., Swings J., De Vos P.;
RT   "Virgibacillus carmonensis sp. nov., Virgibacillus necropolis sp. nov.
RT   and Virgibacillus picturae sp. nov., three novel species isolated from
RT   deteriorated mural paintings, transfer of the species of the genus
RT   salibacillus to Virgibacillus, as Virgibacillus marismortui comb. nov.
RT   and Virgibacillus salexigens comb. nov., and emended description of
RT   the genus Virgibacillus.";
RL   Int. J. Syst. Evol. Microbiol. 53:501-511(2003).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_00165}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC         ChEBI:CHEBI:456216; EC=2.7.4.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00165, ECO:0000256|SAAS:SAAS01114966};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000256|SAAS:SAAS01070220}.
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DR   EMBL; CP022437; ASN03763.1; -; Genomic_DNA.
DR   KEGG; vne:CFK40_01460; -.
DR   KO; K00943; -.
DR   BioCyc; GCF_002224365:CFK40_RS01460-MONOMER; -.
DR   Proteomes; UP000204391; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018095; Thymidylate_kin_CS.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070209}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000204391};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070206, ECO:0000313|EMBL:ASN03763.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070211};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070205};
KW   Reference proteome {ECO:0000313|Proteomes:UP000204391};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165,
KW   ECO:0000256|SAAS:SAAS01070204}.
FT   DOMAIN        8    196       Thymidylate_kin. {ECO:0000259|Pfam:
FT                                PF02223}.
FT   NP_BIND      10     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00165}.
FT   COILED      140    160       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   214 AA;  24606 MW;  4634023E88D08B30 CRC64;
     MSGYFITLEG GEGAGKTSVL QLLEQTLLEK GFDVLATREP GGIEIAEKIR HIILDPVHTA
     MDSRTEALLY AAARRQHLME KVLPALEQGK IVLCDRFIDS SLAYQGYARG LGIDEVFAIN
     QFAIQNCMPD LTLFFDIEPK KGLERIIANK DREKNRLDLE ELHFHEQVYK AYHLLVKKFP
     KRIQIIDAEQ SLEQVNIQVM KKIERFIQFK DYKI
//
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